1NZA

Divalent cation tolerance protein (Cut A1) from thermus thermophilus HB8

Summary for 1NZA

• Entry DOI: 10.2210/pdb1nza/pdb
• Descriptor: Divalent cation tolerance protein, SODIUM ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: cuta, cellular tolerance, monomer, structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm (By similarity): Q7SIA8
• Total number of polymer chains: 1
• Total formula weight: 12011.39

Authors

Bagautdinov, B.,Miyano, M.,Tahirov, T.H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-02-17, release date: 2003-03-11, Last modification date: 2023-10-25)

Primary citation

Bagautdinov, B.
The structures of the CutA1 proteins from Thermus thermophilus and Pyrococcus horikoshii: characterization of metal-binding sites and metal-induced assembly.
Acta Crystallogr.,Sect.F, 70:404-413, 2014

PubMed Abstract: CutA1 (copper tolerance A1) is a widespread cytoplasmic protein found in archaea, bacteria, plants and animals, including humans. In Escherichia coli it is implicated in divalent metal tolerance, while the mammalian CutA1 homologue has been proposed to mediate brain enzyme acetylcholinesterase activity and copper homeostasis. The X-ray structures of CutA1 from the thermophilic bacterium Thermus thermophilus (TtCutA1) with and without bound Na(+) at 1.7 and 1.9 Å resolution, respectively, and from the hyperthermophilic archaeon Pyrococcus horikoshii (PhCutA1) in complex with Na(+) at 1.8 Å resolution have been determined. Both are short and rigid proteins of about 12 kDa that form intertwined compact trimers in the crystal and solution. The main difference in the structures is a wide-type β-bulge on top of the TtCutA1 trimer. It affords a mechanism for lodging a single-residue insertion in the middle of β2 while preserving the interprotomer main-chain hydrogen-bonding network. The liganded forms of the proteins provide new structural information about the metal-binding sites and CutA1 assembly. The Na(+)-TtCutA1 structure unveils a dodecameric assembly with metal ions in the trimer-trimer interfaces and the lateral clefts of the trimer. For Na(+)-PhCutA1, the metal ion associated with six waters in an octahedral geometry. The structures suggest that CutA1 may contribute to regulating intracellular metal homeostasis through various binding modes.

PubMed: 24699729
DOI: 10.1107/S2053230X14003422

Experimental method

X-RAY DIFFRACTION (1.7 Å)